GANAB_MOUSE
ID GANAB_MOUSE Reviewed; 944 AA.
AC Q8BHN3; O08794; Q149A6; Q80U81; Q9CS53;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Neutral alpha-glucosidase AB;
DE EC=3.2.1.207 {ECO:0000269|PubMed:27462106};
DE AltName: Full=Alpha-glucosidase 2;
DE AltName: Full=Glucosidase II subunit alpha {ECO:0000303|PubMed:27462106};
DE Flags: Precursor;
GN Name=Ganab {ECO:0000303|PubMed:28375157, ECO:0000312|MGI:MGI:1097667};
GN Synonyms=G2an, Kiaa0088;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 33-50; 176-187;
RP 823-839 AND 895-905, HETERODIMERIZATION WITH PRKCSH, INTERACTION WITH
RP PTPRC, AND SUBUNIT.
RC TISSUE=T-cell lymphoma;
RX PubMed=9148925; DOI=10.1074/jbc.272.20.13117;
RA Arendt C.W., Ostergaard H.L.;
RT "Identification of the CD45-associated 116-kDa and 80-kDa proteins as the
RT alpha- and beta-subunits of alpha-glucosidase II.";
RL J. Biol. Chem. 272:13117-13125(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 62-96; 134-173; 338-354; 378-400; 438-459; 591-610;
RP 654-662; 685-698; 785-805; 864-880; 892-908 AND 915-944, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH GLYCOSYLATED PTPRC, SUBUNIT, AND GLYCOSYLATION.
RX PubMed=10921916; DOI=10.1074/jbc.m003088200;
RA Baldwin T.A., Gogela-Spehar M., Ostergaard H.L.;
RT "Specific isoforms of the resident endoplasmic reticulum protein
RT glucosidase II associate with the CD45 protein-tyrosine phosphatase via a
RT lectin-like interaction.";
RL J. Biol. Chem. 275:32071-32076(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8] {ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O, ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR, ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE, ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 33-944 IN COMPLEX WITH SUBSTRATE
RP ANALOG AND DEOXYNOJIRIMYCIN, FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION AT ASN-97, DISULFIDE
RP BONDS, MUTAGENESIS OF ASP-542; ASP-618 AND ARG-818, AND ACTIVE SITE.
RX PubMed=27462106; DOI=10.1073/pnas.1604463113;
RA Caputo A.T., Alonzi D.S., Marti L., Reca I.B., Kiappes J.L., Struwe W.B.,
RA Cross A., Basu S., Lowe E.D., Darlot B., Santino A., Roversi P.,
RA Zitzmann N.;
RT "Structures of mammalian ER alpha-glucosidase II capture the binding modes
RT of broad-spectrum iminosugar antivirals.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4630-E4638(2016).
RN [9]
RP FUNCTION.
RX PubMed=28375157; DOI=10.1172/jci90129;
RA Besse W., Dong K., Choi J., Punia S., Fedeles S.V., Choi M.,
RA Gallagher A.R., Huang E.B., Gulati A., Knight J., Mane S., Tahvanainen E.,
RA Tahvanainen P., Sanna-Cherchi S., Lifton R.P., Watnick T., Pei Y.P.,
RA Torres V.E., Somlo S.;
RT "Isolated polycystic liver disease genes define effectors of polycystin-1
RT function.";
RL J. Clin. Invest. 127:1772-1785(2017).
CC -!- FUNCTION: Catalytic subunit of glucosidase II that cleaves sequentially
CC the 2 innermost alpha-1,3-linked glucose residues from the
CC Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature
CC glycoproteins (PubMed:27462106). Required for PKD1/Polycystin-1 and
CC PKD2/Polycystin-2 maturation and localization to the cell surface and
CC cilia (PubMed:28375157). {ECO:0000269|PubMed:27462106,
CC ECO:0000269|PubMed:28375157}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] (N-glucan mannose isomer 9A1,2,3B1,2,3);
CC Xref=Rhea:RHEA:56000, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59080,
CC ChEBI:CHEBI:139493; EC=3.2.1.207;
CC Evidence={ECO:0000269|PubMed:27462106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-
CC asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc)-L-asparaginyl-[protein]; Xref=Rhea:RHEA:55996,
CC Rhea:RHEA-COMP:14355, Rhea:RHEA-COMP:14357, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:59080, ChEBI:CHEBI:59082;
CC EC=3.2.1.207; Evidence={ECO:0000269|PubMed:27462106};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 - 7.;
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC {ECO:0000269|PubMed:27462106}.
CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a beta
CC subunit (PRKCSH) (PubMed:9148925, PubMed:10921916, PubMed:27462106).
CC Binds glycosylated PTPRC (PubMed:9148925, PubMed:10921916).
CC {ECO:0000269|PubMed:10921916, ECO:0000269|PubMed:27462106,
CC ECO:0000269|PubMed:9148925}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q14697}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P79403}. Melanosome
CC {ECO:0000250|UniProtKB:Q14697}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BHN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHN3-2; Sequence=VSP_010676;
CC Name=3;
CC IsoId=Q8BHN3-3; Sequence=VSP_010675;
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65483.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U92793; AAC53182.1; -; mRNA.
DR EMBL; AK017873; BAB30982.1; -; mRNA.
DR EMBL; AK030722; BAC27099.1; -; mRNA.
DR EMBL; AK081915; BAC38370.1; -; mRNA.
DR EMBL; AK122201; BAC65483.1; ALT_INIT; mRNA.
DR EMBL; BC094437; AAH94437.1; -; mRNA.
DR EMBL; BC117888; AAI17889.1; -; mRNA.
DR EMBL; BC117889; AAI17890.1; -; mRNA.
DR CCDS; CCDS29557.1; -. [Q8BHN3-2]
DR CCDS; CCDS89335.1; -. [Q8BHN3-1]
DR RefSeq; NP_001280550.1; NM_001293621.1. [Q8BHN3-1]
DR RefSeq; NP_032086.1; NM_008060.2. [Q8BHN3-2]
DR PDB; 5F0E; X-ray; 1.74 A; A=33-944.
DR PDB; 5H9O; X-ray; 2.37 A; A/C=33-944.
DR PDB; 5HJO; X-ray; 2.29 A; A/C=33-922.
DR PDB; 5HJR; X-ray; 2.40 A; A/C=33-922.
DR PDB; 5IED; X-ray; 1.81 A; A=33-944.
DR PDB; 5IEE; X-ray; 1.92 A; A=33-944.
DR PDB; 5IEF; X-ray; 2.38 A; A=33-944.
DR PDB; 5IEG; X-ray; 1.82 A; A=33-944.
DR PDB; 7KAD; X-ray; 2.51 A; A/C=33-944.
DR PDB; 7KB6; X-ray; 2.20 A; A/C=33-944.
DR PDB; 7KB8; X-ray; 2.38 A; A/C=33-944.
DR PDB; 7KBJ; X-ray; 2.21 A; A/C=348-944, G/I=33-185, H/J=222-328.
DR PDB; 7KBR; X-ray; 2.09 A; A/C=348-944, G/I=33-184, H/J=222-328.
DR PDB; 7KRY; X-ray; 2.55 A; A/C=33-944.
DR PDB; 7L9E; X-ray; 2.29 A; A/C=348-944, E/G=33-185, F/H=222-328.
DR PDBsum; 5F0E; -.
DR PDBsum; 5H9O; -.
DR PDBsum; 5HJO; -.
DR PDBsum; 5HJR; -.
DR PDBsum; 5IED; -.
DR PDBsum; 5IEE; -.
DR PDBsum; 5IEF; -.
DR PDBsum; 5IEG; -.
DR PDBsum; 7KAD; -.
DR PDBsum; 7KB6; -.
DR PDBsum; 7KB8; -.
DR PDBsum; 7KBJ; -.
DR PDBsum; 7KBR; -.
DR PDBsum; 7KRY; -.
DR PDBsum; 7L9E; -.
DR AlphaFoldDB; Q8BHN3; -.
DR SMR; Q8BHN3; -.
DR BioGRID; 199786; 15.
DR IntAct; Q8BHN3; 2.
DR MINT; Q8BHN3; -.
DR STRING; 10090.ENSMUSP00000093965; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR CarbonylDB; Q8BHN3; -.
DR GlyGen; Q8BHN3; 1 site.
DR iPTMnet; Q8BHN3; -.
DR PhosphoSitePlus; Q8BHN3; -.
DR SwissPalm; Q8BHN3; -.
DR EPD; Q8BHN3; -.
DR jPOST; Q8BHN3; -.
DR MaxQB; Q8BHN3; -.
DR PaxDb; Q8BHN3; -.
DR PeptideAtlas; Q8BHN3; -.
DR PRIDE; Q8BHN3; -.
DR ProteomicsDB; 271659; -. [Q8BHN3-1]
DR ProteomicsDB; 271660; -. [Q8BHN3-2]
DR ProteomicsDB; 271661; -. [Q8BHN3-3]
DR Antibodypedia; 14863; 190 antibodies from 28 providers.
DR DNASU; 14376; -.
DR Ensembl; ENSMUST00000096246; ENSMUSP00000093965; ENSMUSG00000071650. [Q8BHN3-2]
DR Ensembl; ENSMUST00000235274; ENSMUSP00000158122; ENSMUSG00000071650. [Q8BHN3-1]
DR GeneID; 14376; -.
DR KEGG; mmu:14376; -.
DR UCSC; uc008gnx.2; mouse. [Q8BHN3-1]
DR CTD; 23193; -.
DR MGI; MGI:1097667; Ganab.
DR VEuPathDB; HostDB:ENSMUSG00000071650; -.
DR eggNOG; KOG1066; Eukaryota.
DR GeneTree; ENSGT00940000159139; -.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; Q8BHN3; -.
DR OMA; QAGIWYP; -.
DR PhylomeDB; Q8BHN3; -.
DR TreeFam; TF300337; -.
DR BRENDA; 3.2.1.207; 3474.
DR UniPathway; UPA00957; -.
DR BioGRID-ORCS; 14376; 16 hits in 72 CRISPR screens.
DR ChiTaRS; Ganab; mouse.
DR PRO; PR:Q8BHN3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BHN3; protein.
DR Bgee; ENSMUSG00000071650; Expressed in embryonic brain and 266 other tissues.
DR ExpressionAtlas; Q8BHN3; baseline and differential.
DR Genevisible; Q8BHN3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:MGI.
DR GO; GO:0017177; C:glucosidase II complex; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0090599; F:alpha-glucosidase activity; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0015926; F:glucosidase activity; ISO:MGI.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IDA:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Golgi apparatus; Hydrolase; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:9148925"
FT CHAIN 33..944
FT /note="Neutral alpha-glucosidase AB"
FT /id="PRO_0000018572"
FT REGION 180..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 542
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066,
FT ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5HJR"
FT ACT_SITE 618
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:27462106"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27462106,
FT ECO:0007744|PDB:5HJO"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27462106,
FT ECO:0007744|PDB:5HJO"
FT BINDING 602
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27462106,
FT ECO:0007744|PDB:5HJO"
FT BINDING 676
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27462106,
FT ECO:0007744|PDB:5HJO"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14697"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10921916,
FT ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5F0E,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT DISULFID 41..47
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT DISULFID 633..644
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT VAR_SEQ 1..252
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_010675"
FT VAR_SEQ 187
FT /note="P -> PFSDKVSLALGSVWDKIKNLFSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9148925"
FT /id="VSP_010676"
FT MUTAGEN 542
FT /note="D->E,N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:27462106"
FT MUTAGEN 618
FT /note="D->N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:27462106"
FT MUTAGEN 818
FT /note="R->E: Disrupts interaction with PRKCSH. Nearly
FT abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:27462106"
FT CONFLICT 647
FT /note="D -> N (in Ref. 2; BAB30982)"
FT /evidence="ECO:0000305"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 59..69
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 350..360
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 372..383
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 406..418
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 449..458
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 478..485
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 515..524
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 544..546
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 575..589
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 623..638
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 657..667
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 670..675
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 691..706
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 708..721
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 729..732
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 764..769
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 775..778
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 784..794
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 802..805
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 808..812
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 820..823
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 828..833
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 840..846
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 849..851
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 853..856
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 861..868
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 871..877
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 888..895
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 901..907
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 913..915
FT /evidence="ECO:0007829|PDB:7KBR"
FT STRAND 917..920
FT /evidence="ECO:0007829|PDB:5F0E"
FT TURN 921..924
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 925..929
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 939..944
FT /evidence="ECO:0007829|PDB:5F0E"
SQ SEQUENCE 944 AA; 106911 MW; 01489861A537416E CRC64;
MAAIAAVAAR RRRSWLSLVL AYLGVCLGIT LAVDRSNFKT CDESSFCKRQ RSIRPGLSPY
RALLDTLQLG PDALTVHLIH EVTKVLLVLE LQGLQKNMTR IRIDELEPRR PRYRVPDVLV
ADPPTARLSV SGRDDNSVEL TVAEGPYKII LTAQPFRLDL LEDRSLLLSV NARGLMAFEH
QRAPRVPQES KDPAEGNGAQ PEATPGDGDK PEETQEKAEK DEPGAWEETF KTHSDSKPYG
PTSVGLDFSL PGMEHVYGIP EHADSLRLKV TEGGEPYRLY NLDVFQYELN NPMALYGSVP
VLLAHSFHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMLD YLQGSGETPQ TDIRWMSESG
IIDVFLMLGP SVFDVFRQYA SLTGTQALPP LFSLGYHQSR WNYRDEADVL EVDQGFDDHN
MPCDVIWLDI EHADGKRYFT WDPTRFPQPL NMLEHLASKR RKLVAIVDPH IKVDSGYRVH
EELRNHGLYV KTRDGSDYEG WCWPGSASYP DFTNPRMRAW WSNMFSFDNY EGSAPNLYVW
NDMNEPSVFN GPEVTMLKDA VHYGGWEHRD IHNIYGLYVH MATADGLIQR SGGIERPFVL
SRAFFSGSQR FGAVWTGDNT AEWDHLKISI PMCLSLALVG LSFCGADVGG FFKNPEPELL
VRWYQMGAYQ PFFRAHAHLD TGRREPWLLA SQYQDAIRDA LFQRYSLLPF WYTLFYQAHK
EGFPVMRPLW VQYPEDMSTF SIEDQFMLGD ALLIHPVSDA GAHGVQVYLP GQEEVWYDIQ
SYQKHHGPQT LYLPVTLSSI PVFQRGGTIV PRWMRVRRSS DCMKDDPITL FVALSPQGTA
QGELFLDDGH TFNYQTRHEF LLRRFSFSGS TLVSSSADPK GHLETPIWIE RVVIMGAGKP
AAVVLQTKGS PESRLSFQHD PETSVLILRK PGVSVASDWS IHLR
